ID   GOLS2_AJURE             Reviewed;         292 AA.
AC   Q9XGN3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Galactinol synthase 2;
DE            Short=ArGolS2;
DE            Short=GolS-2;
DE            EC=2.4.1.123;
DE   Flags: Fragment;
GN   Name=GOLS2;
OS   Ajuga reptans (Bugle).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Ajugoideae; Ajugeae; Ajuga.
OX   NCBI_TaxID=38596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY
RP   COLD, AND CATALYTIC ACTIVITY.
RX   PubMed=10758476; DOI=10.1046/j.1365-313x.2000.00671.x;
RA   Sprenger N., Keller F.;
RT   "Allocation of raffinose family oligosaccharides to transport and storage
RT   pools in Ajuga reptans: the roles of two distinct galactinol synthases.";
RL   Plant J. 21:249-258(2000).
CC   -!- FUNCTION: May promote plant stress tolerance (By similarity).
CC       Galactinol synthase mainly involved in the biosynthesis of transport
CC       raffinose family oligosaccharides (RFOs) that function as
CC       osmoprotectants. {ECO:0000250, ECO:0000269|PubMed:10758476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-
CC         (1->3)-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:12464,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:17505,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.123;
CC         Evidence={ECO:0000269|PubMed:10758476};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Present in phloem-associated intermediary cells.
CC       Weakly expressed in leaves. {ECO:0000269|PubMed:10758476}.
CC   -!- INDUCTION: By cold. Follows a circadian rhythm; accumulates mostly at
CC       the dark phase transition. {ECO:0000269|PubMed:10758476}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC       Galactosyltransferase subfamily. {ECO:0000305}.
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DR   EMBL; AJ237694; CAB51534.1; -; mRNA.
DR   AlphaFoldDB; Q9XGN3; -.
DR   SMR; Q9XGN3; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   BRENDA; 2.4.1.123; 222.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047216; F:inositol 3-alpha-galactosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010325; P:raffinose family oligosaccharide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0015773; P:raffinose transport; IDA:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW   Glycosyltransferase; Manganese; Metal-binding; Transferase.
FT   CHAIN           <1..292
FT                   /note="Galactinol synthase 2"
FT                   /id="PRO_0000418656"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   292 AA;  33768 MW;  7297EBC070771C2B CRC64;
     VGLAKGLRKV GTIYPLVVAV LPDVPPEHRR ILVEQGCVVR EIEPVYPPEN HTEFAMAYYV
     INYSKLRIWE FVEYSKMIYL DGDIQVFENI DHLFDLENGY FYAVMDCFCE KTWSHTPQYQ
     IGYCQQSPKR VHWPKQLGPK PPLYFNAGMF VYEPSLPTYH DLLHTLKITP PTPFAEQDFL
     NMFLRDVYRP IPNVYNLVLA MLWRHPENVN LEAVKVVHYC AAGSKPWRYT GEEENMDRND
     IKMLVNKWRD IYDDEMLDYN AVADPAADGL QLTAVLTEAA GVVRFIPAPS AA